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1OH4

Structural and thermodynamic dissection of specific mannan recognition by a carbohydrate-binding module

Summary for 1OH4
Entry DOI10.2210/pdb1oh4/pdb
Related1OF3 1OF4
DescriptorBETA-MANNOSIDASE, beta-D-mannopyranose-(1-4)-[alpha-D-galactopyranose-(1-6)]beta-D-mannopyranose-(1-4)-[alpha-D-galactopyranose-(1-6)]beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-beta-D-mannopyranose, GLYCEROL, ... (6 entities in total)
Functional Keywordshydrolase, carbohydrate binding module, mannan, lectin, glycoside hydrolase
Biological sourceTHERMOTOGA MARITIMA
Total number of polymer chains1
Total formula weight21962.35
Authors
Boraston, A.B.,Revett, T.J.,Boraston, C.M.,Nurizzo, D.,Davies, G.J. (deposition date: 2003-05-21, release date: 2004-03-16, Last modification date: 2023-12-13)
Primary citationBoraston, A.B.,Revett, T.J.,Boraston, C.M.,Nurizzo, D.,Davies, G.J.
Structural and Thermodynamic Dissection of Specific Mannan Recognition by a Carbohydrate Binding Module, Tmcbm27
Structure, 11:665-, 2003
Cited by
PubMed Abstract: The C-terminal 176 amino acids of a Thermotoga maritima mannanase (Man5) constitute a carbohydrate binding module (CBM) that has been classified into CBM family 27. The isolated CBM27 domain, named TmCBM27, binds tightly (K(a)s 10(5)-10(6) M(-1)) to beta-1, 4-mannooligosaccharides, carob galactomannan, and konjac glucomannan, but not to cellulose (insoluble and soluble) or soluble birchwood xylan. The X-ray crystal structures of native TmCBM27, a TmCBM27-mannohexaose complex, and a TmCBM27-6(3),6(4)-alpha-D-galactosyl-mannopentaose complex at 2.0 A, 1.6 A, and 1.35 A, respectively, reveal the basis of TmCBM27's specificity for mannans. In particular, the latter complex, which is the first structure of a CBM in complex with a branched plant cell wall polysaccharide, illustrates how the architecture of the binding site can influence the recognition of naturally substituted polysaccharides.
PubMed: 12791255
DOI: 10.1016/S0969-2126(03)00100-X
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.35 Å)
Structure validation

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